Journal
ONCOGENE
Volume 27, Issue 42, Pages 5543-5553Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/onc.2008.176
Keywords
YB-1; Twist; p53; GST-fusion protein array; membrane pull-down assay
Funding
- Ministry of Education, Culture, Sports, Science, and Technology of Japan (Mext) [13218132, 17590257]
- Kobayashi Institute for Innovative Cancer Chemotherapy
- grant-in-aid for Cancer Research from the Fukuoka Cancer Society, Japan
- Grants-in-Aid for Scientific Research [17590257, 13218132] Funding Source: KAKEN
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Twist is basic helix-loop-helix transcription factor that binds to E-boxes in gene promoters. Twist possesses an oncogenic function by interfering with the tumor suppressor function of p53. Using a membrane pull-down assay, we found that Twist directly interacts with p53 and that this interaction underlies the inhibitory effects on p53 target gene expression. Twist interacted with the DNA-binding domain of p53 and suppressed the DNA-binding activity of p53. Transcriptional activation of the p21 promoter by p53 was significantly repressed by the expression of Twist. On the other hand, p53 interacted with the N-terminal domain of Twist and repressed Twist-dependent YB-1 promoter activity. Importantly, we found that p53-dependent growth suppression was canceled by the expression of either Twist or YB-1. Thus, our data suggest that Twist inhibits p53 function via a direct interaction with p53.
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